一种能使肺炎链球菌感受态刺激肽失活的蛋白质的鉴定。
Identification of a protein that inactivates the competence-stimulating peptide of Streptococcus pneumoniae.
作者信息
Bergé Mathieu, Langen Hanno, Claverys Jean-Pierre, Martin Bernard
机构信息
Laboratoire de Microbiologie et Génétique Moléculaire, UMR 5100 CNRS-Université Paul Sabatier, 31062 Toulouse Cedex, France.
出版信息
J Bacteriol. 2002 Jan;184(2):610-3. doi: 10.1128/JB.184.2.610-613.2002.
Abstract
Competence for genetic transformation of Streptococcus pneumoniae is a transient physiological property inducible by a competence-stimulating peptide (CSP). A 68-kDa CSP-inactivating protein was previously obtained following lithium chloride (LiCl) extraction. By the same protocol, a CSP-inactivating protein was purified and identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry as an endopeptidase, PepO. Analysis of a pepO mutant provided no support for the hypothesis that PepO participates in competence regulation. To reconcile in vitro and in vivo data, we suggest that LiCl treatment results in the release of intracellular molecules, including PepO.
摘要
肺炎链球菌的遗传转化能力是一种由感受态刺激肽（CSP）诱导的短暂生理特性。先前通过氯化锂（LiCl）提取获得了一种68 kDa的CSP失活蛋白。按照相同的方案，纯化了一种CSP失活蛋白，并通过基质辅助激光解吸电离飞行时间质谱鉴定为一种内肽酶，即PepO。对pepO突变体的分析不支持PepO参与感受态调节这一假说。为了协调体外和体内数据，我们认为LiCl处理导致包括PepO在内的细胞内分子释放。
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